Characterization of acetylcholinesterase activity from Drosophila melanogaster

Melanson, S. W.; Yun, Chang-Hyon; Pezzementi, Maureen L.; Pezzementi, Leo

doi:10.1016/0742-8413(85)90096-9

Cited by 10 publications

(2 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1). The sedimentation shift found between low-salt and high-salt detergent conditions appears only to be the consequence of the interaction with the detergent, whose micelles enhance the molecular volume, resulting in a change in the apparent density of the enzyme [1,12,26]. The increase in the molecular volume by interaction with detergent is not negligible, since an average of 106 molecules of detergent aggregate per micelle of Lubrol PX, which corresponds to an absolute molecular mass of 64000 Da [27].…”

Section: Discussionmentioning

confidence: 94%

“…[6,7]), with a major form common to the different species [8]. Some authors have described the existence of a single membrane AChE whose apparent sedimentation coefficient varies from 5.4S to 5.7 S [9-11], whereas others have shown the presence of distinct biochemical variants [6,[12][13][14]. Recent studies carried out in Drosophila melanogaster [15], Tenebrio molitor [16], Pieris brassicae [17,18] and on purified AChE from the housefly Musca domestica [19] have allowed the characterization of globular membrane forms with their hydrophilic counterparts.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Belzunces¹,

Toutant²,

Bounias³

1988

Biochemical Journal

View full text Add to dashboard Cite

The polymorphism of bee acetylcholinesterase was studied by sucrose-gradient-sedimentation analysis and non-denaturing electrophoretic analysis of fresh extracts. Lubrol-containing extracts exhibited only one form, which sedimented at 5 S when analysed on high-salt Lubrol-containing gradients and 6 S when analysed on low-salt Lubrol-containing gradients. The 5 S/6 S form aggregated upon removal of the detergent when sedimented on detergent-free gradients and was recovered in the detergent phase after Triton X-114 phase separation. Thus the 5 S/6 S enzyme corresponds to an amphiphilic acetylcholinesterase form. In detergent-free extracts three forms, whose apparent sedimentation coefficients are 14 S, 11 S and 7 S, were observed when sedimentations were performed on detergent-free gradients. Sedimentation analyses on detergent-containing gradients showed only a 5 S peak in high-salt detergent-free extracts and a 6 S peak, with a shoulder at about 7 S, in low-salt detergent-free extracts. Electrophoretic analysis in the presence of detergent demonstrated that the 14 S and 11 S peaks corresponded to aggregates of the 5 S/6 S form, whereas the 7 S peak corresponded to a hydrophilic acetylcholinesterase form which was recovered in the aqueous phase following Triton X-114 phase separation. The 5 S/6 S amphiphilic form could be converted into a 7.1 S hydrophilic form by phosphatidylinositol-specific phospholipase C digestion.

show abstract

Section: Discussionmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Belzunces¹,

Toutant²,

Bounias³

1988

Biochemical Journal

View full text Add to dashboard Cite

show abstract

Developmental changes and acetylcholinesterase activity in the metamorphosing brain of Tenebrio molitor: Correlation to ecdysteroid titers

Lenoir-Rousseaux

Delbecque

Gautron³

1994

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

The brain of Tenebrio molitor exhibited marked fluctuations in acetylcholinesterase (AChE) activity throughout metamorphosis. This was true AChE activity, since it was inhibited by high substrate concentrations and by 10 pM of the specific AChE inhibitor BW284C51 [(I ,5-bis'4-allyldimethylammoniumphenyl)-pentan-3-one dibromide] but not by iso-OMPA (tetraisopropylpyrophosphoramide), a cholinesterase (but not AChE) inhibitor. The histochemical AChE activity was localized in the neuropile and the nuclear envelope of neurons and glial cells. The enzyme extracted from brains with 1 O h Triton X-I 00 and 1 M NaCl sedimented as a single peak in a sucrose density gradient, with a sedimentation coefficient of 5.4s. This single AChE sedimentation peak was mainly due to an amphiphilic dimeric form. AChE activity per brain increased in newly ecdysed pupa. AChE activity per milligram of protein exhibited a peak in the mid-pupa which could be correlated to the increase in ecdysteroid titers. o 1994 WiIey-Liss, Inc.

show abstract

The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader.

Hall¹,

Spierer²

1986

The EMBO Journal

263

139

View full text Add to dashboard Cite

The Ace locus of Drosophila melanogaster has been mapped at the molecular level. cDNA clones from the locus have been isolated and their sequence determined, confirming that Ace forms the structural gene for acetylcholinesterase (AChE). The cDNAs have a 1950 nucleotide open reading frame from which the complete amino acid sequence of AChE has been deduced. The Drosophila enzyme is found to have extensive homology to the known sequence of Torpedo AChE. Ace cDNAs have an unusual structure with a long 5′ leader and several short upstream open reading frames.

show abstract

Characterization of acetylcholinesterase activity from Drosophila melanogaster

Cited by 10 publications

References 24 publications

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Acetylcholinesterase from Apis mellifera head. Evidence for amphiphilic and hydrophilic forms characterized by Triton X-114 phase separation

Developmental changes and acetylcholinesterase activity in the metamorphosing brain of Tenebrio molitor: Correlation to ecdysteroid titers

The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader.

Contact Info

Product

Resources

About